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Protocols

Specificity / Sensitivity

Phospho-Stat3 (Ser727) (6E4) Mouse mAb detects endogenous levels of Stat3 only when phosphorylated at serine 727. It does not significantly cross-react with the corresponding phosphorylated serines of other Stat proteins. The antibody does not cross-react with nonphosphorylated Stat3 or with Stat3 phosphorylated at other sites.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser727 of mouse Stat3.

Western Blotting

Background

The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).